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The Polyphenol Piceid Destabilizes Preformed Amyloid Fibrils and Oligomers In Vitro: Hypothesis on Possible Molecular Mechanisms

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Abstract

Alzheimer’s disease (AD) is characterized by deposits of amyloid in various tissues. The neuronal cytotoxicity of Aβ peptides is attributed not only to various mechanisms but also to amyloid fibrils and soluble oligomeric intermediates. Consequently, finding molecules to prevent or reverse the oligomerization and fibrillization of Aβ could be of therapeutic value in the treatment of AD. We show that piceid, a polyphenol of the stilbene family, destabilized fibrils and oligomers to give back monomers that are not neurotoxic molecules. The mechanism of this destabilization could be a dynamic interaction between the polyphenol and the Aβ that could open the hydrophobic zipper and shift the reversible equilibrium “random coil⇔β-sheet” to the disordered structure.

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Acknowledgments

We are grateful to SERCOMI for Electron Microscopy and to Dr. Ray Cooke for reading the manuscript. Financial support for this study came in part from the “Conseil Régional d’Aquitaine”.

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Authors and Affiliations

  1. Laboratoire de physique et biophysique, GESVAB EA 3675, ISVV, Université de Bordeaux 2, 146 rue Léo Saignat, 33076, Bordeaux cedex, France

    Céline Rivière, Jean-Claude Delaunay & Jean-Pierre Monti

  2. UMR 5095 CNRS, IBGC, Université Bordeaux 2, 1 rue Camille Saint Saens, 33077, Bordeaux cedex, France

    Françoise Immel & Christophe Cullin

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  1. Céline Rivière
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  2. Jean-Claude Delaunay
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  3. Françoise Immel
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Correspondence to Jean-Pierre Monti.

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Rivière, C., Delaunay, JC., Immel, F. et al. The Polyphenol Piceid Destabilizes Preformed Amyloid Fibrils and Oligomers In Vitro: Hypothesis on Possible Molecular Mechanisms. Neurochem Res 34, 1120–1128 (2009). https://doi.org/10.1007/s11064-008-9883-6

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